GPI Membrane Anchors

Author: Almeida   M  

Publisher: Elsevier Science‎

Publication year: 2012

E-ISBN: 9780323156097

P-ISBN(Paperback): 9780121593902

P-ISBN(Hardback):  9780121593902

Subject: Q24 cell morphology

Language: ENG

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Description

GPI Membrane Anchors reviews major advances in our understanding of glycosylphosphatidylinositol (GPI) membrane anchors. The book examines the GPI structure and its originality as an anchoring device, its ubiquitous distribution, the main steps of its biosynthetic pathway, and the elegant means by which a protein signals for GPI attachment. It also presents evidence for the uniqueness of GPI as a tag in intracellular traffic and as a mediator of transmembrane signaling.
This volume is organized into 20 chapters and begins with a discussion of the structural requirements of a nascent protein for processing to a PI-G anchored form, with emphasis on experiments on intact cells and cell-free systems. It then turns to the mechanisms underlying signal transduction by GPI-anchored membrane proteins, the LY-6 superfamily of GPI-anchored molecules, and glycosylated-phosphatidylinositols as virulence factors in Leishmania. The reader is also introduced to the molecular biology of GPI-anchored border hydrolases, the role of GPIs and their inositolglycan derivatives in the mediation of insulin and growth factor function, and biosynthesis and cellular localization of GPI-modified glycoproteins in Saccharomyces cerevisiae. An account of electrospray mass spectrometry of a C-terminal peptide purified from the scrapie isoform of the scrapie prion protein is also given. The book concludes with a chapter on GPI-anchored recognition molecules that function in axonal fasciculation, growth, a

Chapter

Front Cover

pp.:  1 – 2

Dedication

pp.:  2 – 4

GPI Membrane Anchors

pp.:  2 – 3

Copyright Page

pp.:  3 – 10

Contributors

pp.:  4 – 8

Preface

pp.:  8 – 12

Table of Contents

pp.:  10 – 2

CHAPTER 2. SIGNAL TRANSDUCTION BY GPI-ANCHORED MEMBRANE PROTEINS

pp.:  33 – 40

CHAPTER 3. EMERGENCE OF THE LY-6 SUPERFAMILY OF GPI-ANCHORED MOLECULES

pp.:  40 – 49

CHAPTER 4. GLYCOSYLATED-PHOSPHATIDYLINOSITOLS AS VIRULENCE FACTORS IN LEISHMANIA

pp.:  49 – 69

CHAPTER 5. WHY DO SO MANY SURFACE PROTEINS OF TRYPANOSOMATIDS HAVE GPI-ANCHORS?

pp.:  69 – 84

CHAPTER 6. PROBING THE SIGNAL FOR GLYCOPHOSPHATIDYLINOSITOL ANCHOR ATTACHMENT USING DECAY ACCELERATING FACTOR AS A MODEL SYSTEM

pp.:  84 – 96

CHAPTER 7. INOSITOLGLYCANS AND CELLULAR SIGNALLING

pp.:  96 – 122

CHAPTER 8. ELECTROSPRAY MASS SPECTROMETRY OF THE GLYCOSYIINOSITOL PHOSPHOLIPID OF THE SCRAPIE PRION PROTEIN

pp.:  122 – 132

CHAPTER 9. BIOSYNTHESIS OF GLYCOPHOSPHOINOSITOL ANCHORS IN SACCHAROMYCES CEREVISIAE

pp.:  132 – 143

CHAPTER 10. CHARACTERIZATION OF THE PLASMA GLYCOSYLPHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE D (GPI-PLD)

pp.:  143 – 151

CHAPTER 11. EVOLUTIONARY ASPECTS OF GPI METABOLISM IN KINETOPLASTID PARASITES

pp.:  151 – 166

CHAPTER 12. BIOSYNTHESIS OF GLYCOSYL-PHOSPHATIDYLINOSITOL

pp.:  166 – 181

CHAPTER 13. POLARIZED SORTING OF GPI-LINKED PROTEINS IN EPITHELIA AND MEMBRANE MICRODOMAINS

pp.:  181 – 208

CHAPTER 14. EVALUATION OF SOMATIC CELL VARIANTS DEFICIENT IN GLYCOSYLPHOSPHATIDYL-INOSITOL ANCHORING AS CANDIDATES FOR GENETIC CORRECTION

pp.:  208 – 222

CHAPTER 15. BIOCHEMICAL AND FUNCTIONAL CHARACTERIZATION OF A GLYCOLIPID ANCHORED CELL ADHESION MOLECULE IN DICTYOSTELIUM DISCOIDEUM

pp.:  222 – 240

CHAPTER 16. THE MOLECULAR BIOLOGY OF GPI-ANCHORED BORDER HYDROLASES

pp.:  240 – 257

CHAPTER 17.THE BIOLOGY OF THE GLYCOSYLPHOSPHATIDYLINOSITOL-SPECIFIC PHOSPHOLIPASE C OF TRYPANOSOMA BRUCEI

pp.:  257 – 271

CHAPTER 18. BACTERIAL PIPLCS - UNIQUE PROPERTIES AND USEFULNESS IN STUDIES ON GPI ANCHORS

pp.:  271 – 287

CHAPTER 19. A CHEMICAL MODIFICATION THAT MAKES GLYCOINOSITOL PHOSPHOLIPIDS RESISTANT TO PHOSPHOLIPASE C CLEAVAGE: FATTY ACID ACYLATION OF INOSITOL

pp.:  287 – 305

CHAPTER 20. GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED RECOGNITION MOLECULES THAT FUNCTION IN AXONAL FASCICULATION, GROWTH AND GUIDANCE IN THE NERVOUS SYSTEM

pp.:  305 – 321

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